Protein engineering as a strategy to avoid formation of amyloid fibrils
about
High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein designNMR solution structure of the activation domain of human procarboxypeptidase A2Sequence determinants of protein aggregation: tools to increase protein solubility.Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domainSDS can be utilized as an amyloid inducer: a case study on diverse proteinsThe impact of extra-domain structures and post-translational modifications in the folding/misfolding behaviour of the third PDZ domain of MAGUK neuronal protein PSD-95.Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.Differential effects of glycation on protein aggregation and amyloid formation.Investigation of the molecular similarity in closely related protein systems: The PrP case study.Using simple artificial intelligence methods for predicting amyloidogenesis in antibodiesSequence determinants of amyloid fibril formationLarge proteins have a great tendency to aggregate but a low propensity to form amyloid fibrilsRational design of aggregation-resistant bioactive peptides: reengineering human calcitonin.EVA: large-scale analysis of secondary structure prediction.Structured disorder and conformational selection.The interconversion between a flexible β-sheet and a fibril β-arrangement constitutes the main conformational event during misfolding of PSD95-PDZ3 domainPrediction and analysis of antibody amyloidogenesis from sequences.Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments.Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase.Protein aggregation in silico.Exploring amyloid formation by a de novo design.Therapeutic strategies against protein misfolding in neurodegenerative diseases.Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation.A minimal conformational switching-dependent model for amyloid self-assembly.Molecular Insight into Human Lysozyme and Its Ability to Form Amyloid Fibrils in High Concentrations of Sodium Dodecyl Sulfate: A View from Molecular Dynamics SimulationsThe behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation.Oligomerization of amyloid Abeta16-22 peptides using hydrogen bonds and hydrophobicity forces.FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils.Competing intrachain interactions regulate the formation of beta-sheet fibrils in bovine PrP peptides.Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro.Specific interactions of serpins in their native forms attenuate their conformational transitions.Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy.Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state.Amyloid fibril formation can proceed from different conformations of a partially unfolded protein.A designed system for assessing how sequence affects alpha to beta conformational transitions in proteins.Stimulation and inhibition of fibril formation by a peptide in the presence of different concentrations of SDS.Low concentration of guanidine hydrochloride induces the formation of an aggregation-prone state in alpha-urease.Characterization of large amyloid fibers and tapes with Fourier transform infrared (FT-IR) and Raman spectroscopy.Investigating the effects of mutations on protein aggregation in the cell.Rigidity of transmembrane proteins determines their cluster shape.
P2860
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P2860
Protein engineering as a strategy to avoid formation of amyloid fibrils
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
Protein engineering as a strategy to avoid formation of amyloid fibrils
@en
type
label
Protein engineering as a strategy to avoid formation of amyloid fibrils
@en
prefLabel
Protein engineering as a strategy to avoid formation of amyloid fibrils
@en
P2093
P2860
P356
P1433
P1476
Protein engineering as a strategy to avoid formation of amyloid fibrils
@en
P2093
P2860
P304
P356
10.1110/PS.9.9.1700
P577
2000-09-01T00:00:00Z